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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

The 1.23 A structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link.

The structure of Pichia pastoris lysyl oxidase (PPLO) in a new crystal form has been refined at 1.23 A resolution. PPLO, a copper amine oxidase (CuAO) with a 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor, differs from most other members of the CuAO enzyme family in having the ability to oxidize the side chain of lysine residues in a polypeptide. In the asymmetric unit of the crystals, the structure analysis has located residues 43-779 of the polypeptide chain, seven carbohydrate residues, the active-site Cu atom, an imidazole molecule bound at the active site, two buried Ca(2+) ions, five surface Mg(2+) ions, five surface Cl(-) ions and 1045 water molecules. The crystallographic residuals are R = 0.112 and R(free) = 0.146. The TPQ cofactor and several other active-site residues are poorly ordered, in contrast to the surrounding well ordered structure. A covalent cross-link is observed between two lysine residues, Lys778 and Lys66. The cross-link is likely to have been formed by the oxidation of Lys778 followed by a spontaneous reaction with Lys66. The link is modelled as dehydrolysinonorleucine.[1]

References

  1. The 1.23 A structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link. Duff, A.P., Cohen, A.E., Ellis, P.J., Hilmer, K., Langley, D.B., Dooley, D.M., Freeman, H.C., Guss, J.M. Acta Crystallogr. D Biol. Crystallogr. (2006) [Pubmed]
 
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